Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface
about
Structural and Genetic Studies Demonstrate Neurologic Dysfunction in Triosephosphate Isomerase Deficiency Is Associated with Impaired Synaptic Vesicle DynamicsDetermining the molecular mechanism of inactivation by chemical modification of triosephosphate isomerase from the human parasite Giardia lamblia: a study for antiparasitic drug designDifferent contribution of conserved amino acids to the global properties of triosephosphate isomerasesA ribosomal misincorporation of Lys for Arg in human triosephosphate isomerase expressed in Escherichia coli gives rise to two protein populationsThe importance of arginine codons AGA and AGG for the expression in E. coli of triosephosphate isomerase from seven different species.Structural effects of protein aging: terminal marking by deamidation in human triosephosphate isomerase.Progressive dry-core-wet-rim hydration trend in a nested-ring topology of protein binding interfaces.Natural Products as New Treatment Options for Trichomoniasis: A Molecular Docking Investigation.Hsp70- and Hsp90-mediated proteasomal degradation underlies TPI sugarkill pathogenesis in Drosophila.Pyruvate kinase triggers a metabolic feedback loop that controls redox metabolism in respiring cellsStructural and thermodynamic folding characterization of triosephosphate isomerases from Trichomonas vaginalis reveals the role of destabilizing mutations following gene duplication.Triosephosphate isomerase I170V alters catalytic site, enhances stability and induces pathology in a Drosophila model of TPI deficiency.The return of metabolism: biochemistry and physiology of the pentose phosphate pathwaySubstrate-Induced Dimerization of Engineered Monomeric Variants of Triosephosphate Isomerase from Trichomonas vaginalis.Evidence of a triosephosphate isomerase non-catalytic function crucial to behavior and longevityStructural analysis on mutation residues and interfacial water molecules for human TIM disease understandingRed blood cell storage affects the stability of cytosolic native protein complexes.A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease.Structural and thermodynamic characterization of metal binding in Vps29 from Entamoeba histolytica: Implication in retromer function.The role of conserved water molecules in the catalytic domain of protein kinasesTriose phosphate isomerase from the blood fluke Schistosoma mansoni: biochemical characterisation of a potential drug and vaccine target.Molecular interactions of c-ABL mutants in complex with imatinib/nilotinib: a computational study using linear interaction energy (LIE) calculations.Role of bridging water molecules in GSK3β-inhibitor complexes: insights from QM/MM, MD, and molecular docking studies.In Silico Studies of Small Molecule Interactions with Enzymes Reveal Aspects of Catalytic Function
P2860
Q27309025-9706BE3B-952E-44C7-9772-31CE70BF40E3Q27670984-6E4D69A8-B71F-4AC8-BA44-EB817A1B28E9Q27685402-A670C81D-C492-4B52-B243-8EC1D1A4F639Q28478855-617E4C54-C479-4649-9B8A-EA9FD68D83C7Q30360270-45F2DE88-3485-4229-9A00-08C806F6B720Q30373836-D5A5E0ED-9666-4CAF-9216-D8C717E13EBCQ31053281-BE2F3DB5-A2E0-44F0-973A-8A18DB8FF205Q33553302-BDA6176E-8C2A-4A39-98AB-B850F83F31C7Q34204041-9845892D-D0D7-42A0-A83A-7183247E9762Q34215123-714AE59F-6C46-46E8-B334-65E2F7C9DE16Q34348491-2AA7B25A-7049-41A8-A9A9-FBD73D4E1D92Q34714976-7A083EF5-9423-4463-AC7D-9FCBDC38C8B8Q35752267-05A5A2FE-8E52-49EA-A1B1-E57990A8343EQ35855397-F2850ACF-9B2E-4511-A827-1D25139BBD80Q37012024-421E0A50-68A4-4633-AB5B-518582AD2384Q37368236-84656AA3-6BBB-4458-845F-398258BBFF27Q39025400-5442C301-0BA8-4E11-B5AA-49890810EDF7Q39221322-96388FB9-5D14-4841-90B6-4BB73702505DQ40051280-479B883D-104F-4E34-84C7-E4573C7D0E43Q41949035-B4832728-FF85-4F5B-8A65-1C32F28D537AQ45830632-98616055-7667-494E-87D5-2E72F408E57CQ54512250-4DD222DD-B575-4536-9D20-42A77A84FDC0Q54598455-3C211601-2D0E-4947-BA59-D7A88022535CQ58042970-52614DFB-1A6C-4940-9E15-C43CB558AEA7
P2860
Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface
description
2008 nî lūn-bûn
@nan
2008 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Structural basis of human trio ...... network at the dimer interface
@ast
Structural basis of human trio ...... network at the dimer interface
@en
Structural basis of human trio ...... network at the dimer interface
@nl
type
label
Structural basis of human trio ...... network at the dimer interface
@ast
Structural basis of human trio ...... network at the dimer interface
@en
Structural basis of human trio ...... network at the dimer interface
@nl
prefLabel
Structural basis of human trio ...... network at the dimer interface
@ast
Structural basis of human trio ...... network at the dimer interface
@en
Structural basis of human trio ...... network at the dimer interface
@nl
P2093
P2860
P50
P3181
P356
P1476
Structural basis of human trio ...... network at the dimer interface
@en
P2093
Armando Gómez-Puyou
Beatriz Aguirre-López
Claudia Rodríguez-Almazán
Marietta Tuena de Gómez-Puyou
P2860
P304
23254-23263
P3181
P356
10.1074/JBC.M802145200
P407
P577
2008-06-18T00:00:00Z